Alterations of inter-domain flexibility in actin monomers during cyclophosphamide treatment

Abstract The actin is one of the main component eukaryotic cytoskeleton. continuous rearrangement filaments provided by different complexes with divalent cations (Ca 2+ or Mg ) and nucleotides (ATP, ADP). In medical routine, cyclophosphamide (CP) applied as cytostatic it was shown that in vivo muscle filament system changed CP treatment has direct interaction monomers well. evolutionary importance physical links between domains most interesting question to understand multi-domain development protein functions. Here, we analyse thermal stability modifier act inter-domain proteins, monitored DSC, concept how did nucleotide binding cleft two affect activation energy if blocked released dissociation, respectively. We investigated linkers on thermodynamic properties actin. Ca bound G-actin can be stabilized polymerization. -F lacks structural integrity more flexible polymer shows same monomers. However, not show any kinetic response treatment. assume linker reduces which leads a reactive variable structure advantage for